Poly(ethylene terephthalate) (PET) texture was exposed to oxygen plasma glow discharge to produce peroxides on its surfaces. These peroxides were then used as catalysts for the polymerization of acrylic acid (AA) in order to prepare a PET introduced by a carboxylic acid group (PET-A). Chitosan and quaternized chitosan (QC) were then coupled with the carboxyl groups on the PET-A to obtain chitosan-grafted PET (PET-A-C) and QC-grafted PET (PET-A-QC), respectively. These surface-modified PETs were characterized by attenuated total reflection Fourier transform IR spectroscopy, electron spectroscopy for chemical analysis, and a contact angle goniometer. The amounts of AA, chitosan, and QC grafted on the PET surfaces as determined by the gravimetric method were about 6, 8, and 9 g/cm 2 , respectively. The antibacterial activity of the surface-modified PET textures was investigated using a shake flask method. After 6 h of shaking, the growth of bacteria was markedly inhibited by PET with ionically (86% in PET-A Ϫ -C ϩ ) and covalently (75% in PET-A-C) grafted chitosan and with covalently grafted QC (83% in PET-A-QC). After the laundering the inhibition of the growth of the bacteria was maintained in the range of 48 -58%, showing the fastness of the chitosan-grafted PET textures against laundering.
Understanding functional interactions between DCs and antigens is necessary for achieving an optimal and desired immune response during vaccine development. Here, we identified and characterized protein Rv2299c (heat-shock protein 90 family), which effectively induced DC maturation. The Rv2299c-maturated DCs showed increased expression of surface molecules and production of proinflammatory cytokines. Rv2299c induced these effects by binding to TLR4 and stimulating the downstream MyD88-, MAPK- and NF-κB-dependent signaling pathways. The Rv2299c-maturated DCs also showed an induced Th1 cell response with bactericidal activity and expansion of effector/memory T cells. The Rv2299c-ESAT-6 fused protein had greater immunoreactivity than ESAT-6. Furthermore, boosting BCG with the fused protein significantly reduced hypervirulent Mycobacterium tuberculosis HN878 burdens post-challenge. The pathological study of the lung from the challenged mice assured the efficacy of the fused protein. The fused protein boosting also induced Rv2299c-ESAT-6-specific multifunctional CD4+ T-cell response in the lungs of the challenged mice. Our findings suggest that Rv2299c is an excellent candidate for the rational design of an effective multiantigenic TB vaccine.
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